Somatic mutation of the T15 heavy chain gives rise to an antibody with autoantibody specificity.

作者：Betty Diamond, Matthew D. Scharff · 发表于：Proceedings of the National Academy of Sciences · 年份：1984 · DOI：10.1073/pnas.81.18.5841 · 被引用次数：344 · 研究领域：Monoclonal and Polyclonal Antibodies Research、Chronic Lymphocytic Leukemia Research、T-cell and B-cell Immunology

The S107 IgA kappa-chain myeloma cell line makes an antiphosphocholine antibody of the T15 idiotype. A somatic mutant of this line, U4, makes an immunoglobulin with a single amino acid substitution of an alanine for a glutamic acid at residue 35. This single amino acid change results in a loss of phosphocholine binding activity. However, the U4 immunoglobulin has acquired reactivity with a variety of phosphorylated macromolecules, including double-stranded DNA, protamine, and cardiolipin. Thus, a single amino acid change in the T15 heavy chain can transform an antibacterial antibody into an antibody that resembles the autoantibodies seen in mice and man with autoimmune disease.